BINDING OF TRUNCATED PEPTIDES TO THE MHC MOLECULE IAD

被引：9

作者：

DORNMAIR, K

CLARK, BR

MCCONNELL, HM

机构：

[1] STANFORD UNIV,STAUFFER LAB PHYS CHEM,STANFORD,CA 94305

[2] BIOSPAN INC,REDWOOD CITY,CA 94063

来源：

FEBS LETTERS | 1991年 / 294卷 / 03期

关键词：

ANTIGEN PRESENTATION; T-HELPER LYMPHOCYTE;

D O I：

10.1016/0014-5793(91)81439-F

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A peptide comprising amino acids 323-339 of chicken ovalbumin is known to bind to two heterodimeric conformations of the MHC molecule IA(d), and to each of its separate alpha- and beta-chains. We report that minor C- and N-terminal trucations of the parent peptide do not alter the binding pattern. A decrease in binding activity was observed upon deletion of the histidine residues of the already truncated peptides. Peptides as short as 4 amino acids associate weakly with all four proteins.

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页码：244 / 246

页数：3

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